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Binding of uteroglobin to microsomes and plasmatic membranes
Author(s) -
González Keybell Díaz,
Nieto Antonio
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00167-8
Subject(s) - microsome , dithiothreitol , chaps , membrane , chemistry , trypsin , biochemistry , uteroglobin , in vitro , enzyme , chromatography , gene
Microsomes and plasmatic membranes from rat liver bind radioactive uteroglobin (UG) in vitro with high affinity ( K d = 1.7 × 10 −10 M). The binding is saturable and specific and dependent on previous reduction of UG with dithiothreitol. Microsomes from rat spleen or lung or from rabbit endometrium also possess a similar ability. Binding capacity is not affected by previous treatment of microsomes with phospholipase A 2 or peptide‐ N ‐glycosidase F but is lost after brief treatment with trypsin. The complex formed between UG and the binding component can be solubilized from microsomes with 5 mM CHAPS and it elutes with an apparent M r of 90,000 in a Sephacryl 200 column. The complex is resistant to 8 M urea but is completely dissociated by Triton X‐100. The UG‐binding protein(s) has been partially purified from solubilized microsomes and membranes by affinity chromatography. The results are discussed in relation to a possible physiological effect of UG on cellular membranes.